s-allylcysteine and acetyl-aspartyl-glutamyl-valyl-aspartal

s-allylcysteine has been researched along with acetyl-aspartyl-glutamyl-valyl-aspartal* in 1 studies

Other Studies

1 other study(ies) available for s-allylcysteine and acetyl-aspartyl-glutamyl-valyl-aspartal

Article	Year
Protective effect of S-allyl-L-cysteine, a garlic compound, on amyloid beta-protein-induced cell death in nerve growth factor-differentiated PC12 cells. Neuroscience research, 2003, Volume: 46, Issue:1 Aged garlic extract (AGE) contains several neuroactive compounds, including S-allyl-L-cysteine (SAC) and allixin. We characterized cell death induced by amyloid beta-protein (Abeta), 4-hydroxynonenal (HNE), tunicamycin, an endoplasmic reticulum (ER) stressor, or trophic factor deprivation, and investigated whether and how SAC could prevent this in nerve growth factor (NGF)-differentiated PC12 cells, a model of neuronal cells. Exposure of the cells to amyloid beta-protein(1-40) (Abeta(1-40)) decreased the extent of [3-(4,5)-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium (MTT) reduction activity and loss of neuronal integrity, but these effects were not prevented by Ac-DEVD-CHO, a caspase-3 inhibitor. Simultaneously applied SAC protected the cells against Abeta-induced cell death in a concentration-dependent manner. It also protected them against tunicamycin-induced neuronal death. In contrast, it afforded no protection against cell death induced by HNE and trophic factor deprivation, which is mediated by a caspase-3-dependent pathway. These results suggest that SAC may selectively protect cell death induced by Abeta and tunicamycin, which may be triggered by ER dysfunction in NGF-differentiated PC12 cells. Topics: Aldehydes; Amyloid beta-Peptides; Animals; Anti-Bacterial Agents; Cell Death; Cell Differentiation; Cysteine; Cysteine Proteinase Inhibitors; Endoplasmic Reticulum; Garlic; Nerve Growth Factor; Neurons; Neuroprotective Agents; Oligopeptides; PC12 Cells; Rats; Tunicamycin	2003

Article

Year

Protective effect of S-allyl-L-cysteine, a garlic compound, on amyloid beta-protein-induced cell death in nerve growth factor-differentiated PC12 cells.

Neuroscience research, 2003, Volume: 46, Issue:1

Aged garlic extract (AGE) contains several neuroactive compounds, including S-allyl-L-cysteine (SAC) and allixin. We characterized cell death induced by amyloid beta-protein (Abeta), 4-hydroxynonenal (HNE), tunicamycin, an endoplasmic reticulum (ER) stressor, or trophic factor deprivation, and investigated whether and how SAC could prevent this in nerve growth factor (NGF)-differentiated PC12 cells, a model of neuronal cells. Exposure of the cells to amyloid beta-protein(1-40) (Abeta(1-40)) decreased the extent of [3-(4,5)-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium (MTT) reduction activity and loss of neuronal integrity, but these effects were not prevented by Ac-DEVD-CHO, a caspase-3 inhibitor. Simultaneously applied SAC protected the cells against Abeta-induced cell death in a concentration-dependent manner. It also protected them against tunicamycin-induced neuronal death. In contrast, it afforded no protection against cell death induced by HNE and trophic factor deprivation, which is mediated by a caspase-3-dependent pathway. These results suggest that SAC may selectively protect cell death induced by Abeta and tunicamycin, which may be triggered by ER dysfunction in NGF-differentiated PC12 cells.

Topics: Aldehydes; Amyloid beta-Peptides; Animals; Anti-Bacterial Agents; Cell Death; Cell Differentiation; Cysteine; Cysteine Proteinase Inhibitors; Endoplasmic Reticulum; Garlic; Nerve Growth Factor; Neurons; Neuroprotective Agents; Oligopeptides; PC12 Cells; Rats; Tunicamycin

2003